CATH Classification

Domain Context

CATH Clusters

Superfamily 2-enoyl-CoA Hydratase; Chain A, domain 1
Functional Family acetyl-CoA carboxylase isoform X2

Enzyme Information
Acetyl-CoA carboxylase.
based on mapping to UniProt Q13085
ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA.
-!- This enzyme is a multi-domain polypeptide that catalyzes three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyzes the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. -!- In some organisms these activities are catalyzed by separate enzymes (see EC and EC -!- The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.
Biotin carboxylase.
based on mapping to UniProt Q13085
ATP + [biotin carboxyl-carrier protein]-biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]- carboxybiotin-N(6)-L-lysine.
-!- This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC -!- In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). -!- Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyzes the transfer of the carboxyl group from biotin to acetyl-CoA (see EC

UniProtKB Entries (1)

Homo sapiens
Acetyl-CoA carboxylase 1

PDB Structure

External Links
Primary Citation
Crystal Structure of Human Acaca C-Terminal Domain
Froese, D.S., Muniz, J.R.C., Kiyani, W., Krojer, T., Vollmar, M., von Delft, F., Bountra, C., Arrowsmith, C.H., Edwards, A., Oppermann, U., Yue, W.W.
To be Published